Experimental studies of kinesin motor proteins moving along microtubules indicate that these molecular motors interact with each [1]}, [2]}, [3]}. It was argued that these interactions most probably are short-range and relatively weak attractive (\(1.6\pm 0.5 k_{B}T\) ) [1]}. It is reasonable to assume that many other motor proteins have similar properties. At microscopic level, molecular motors are involved in a variety of chemical transitions such as binding to the filament, chemical transformations during the hydrolysis, dissociation from the track [5]}. Intermolecular interactions influence all these processes, suggesting an important role for interactions in the collective behavior of molecular motors. However, the underlying mechanisms are still not well clarified [6]}, [7]}. Existing theoretical studies of cooperative dynamics in interacting molecular motors are mostly phenomenological without quantitative description of relevant chemical processes [8]}, [9]}, [10]}, [11]}.
